ID A0A432DW67_9BURK Unreviewed; 655 AA.
AC A0A432DW67;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=EKL30_02600 {ECO:0000313|EMBL:RTZ47888.1};
OS Candidimonas sp. SYP-B2681.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Candidimonas.
OX NCBI_TaxID=2497686 {ECO:0000313|EMBL:RTZ47888.1, ECO:0000313|Proteomes:UP000288599};
RN [1] {ECO:0000313|EMBL:RTZ47888.1, ECO:0000313|Proteomes:UP000288599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYP-B2681 {ECO:0000313|EMBL:RTZ47888.1,
RC ECO:0000313|Proteomes:UP000288599};
RA Zhang M.-Y., Zhang Y.-X.;
RT "Candidimonas lamiisoli sp. nov., a novel bacterium can accelerate seed
RT germination.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004382}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004382}; Periplasmic side
CC {ECO:0000256|ARBA:ARBA00004382}.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RTZ47888.1}.
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DR EMBL; RYDV01000001; RTZ47888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432DW67; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000288599; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47529; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D; 1.
DR PANTHER; PTHR47529:SF1; PERIPLASMIC CHAPERONE PPID; 1.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:RTZ47888.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000288599};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 266..369
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 70915 MW; AD84173C0F301CDC CRC64;
MFDFIRTHQR LMQLVLLVLI LPSFVLIGVS GYSNYVSGDE PLVKVGDSTI TSQEFDQARR
NQLEQIQQNA QGGFDPAVLD NPAARSVLLE SLIDRRVVAT TATKERFSVS DTALRQAIAS
MPQLQVDGQF SPERYNQVLA SAGLNTRDFE QGQRAELALD RVLGPIALTA SVPAAVVDRL
EHVLTEERTV RLAAFPVSDF EKDLMITDAD IQAWYEKNKQ SLELPEQVSA EYILLNEPAA
MENLPAPTPE DLQKYYEQNK ARYVQPARVN VSHIQISVAT AASDDERAAA RTKAEEIAKK
LSADPSAFAE TARSESQDAG TAKDGGKLGW ITKGSWPANL EQVVFALEKG QVSDAVEGPG
GYHVFQASDI QAEKGESFDE ARSKIEAEVR RQLGAERFAD MATRLTSLVY DNPTSLQPAA
DALGMKIKSA AGIARDRLLP SDEVGANAAS AGEDASLLDD VRVRRALFTQ QALNDKQNSG
VIEISPDTMI VVRVSAVTPA HIPELAKVKS HIQEKLKEEG ALAAAEKAGK DLLATFQNSP
NQTIVPEQFG TPLSISRINA QGLDKPVVDA AFSVSTKKLP QYAGVKGPQG FAVIRIEDAK
PGKTDSPLLA TLPAELNQAW ARAEEQAVLK SMKAEANVKM LPDAQKALAG DTARN
//
